Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP).

Biomedica biochimica acta - 1 Jan 1991

Heinzel-Wieland R, Steffens G J, Flohé L

Abstract excerpt

Tandem gene plasmids were constructed and used to express inactive proteins equivalent to human antileukoproteinase (ALP) and the variants [Leu73]-ALP and [Leu73, 82, 94, 96]-ALP in E. coli K12. After extraction, refolding, and purification, highly pure and active inhibitors were obtained in good yields. Inhibitory constants for human leukocyte elastase and cathepsin G were found to be similar. The variants in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Genetic Variation
Share to Kinetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Plasmids

Share to Proteins

Share to Recombinant Proteins

Source

Identifiers

PMID: 1801742

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP).PMID 1801742Read ↗

The contribution of key hydrophobic residues in ecotin to enzyme-inhibitor complex stability.Semantic proximity Read ↗

Bioengineering: alpha 1-proteinase inhibitor site-specific mutagenesis. The prospect for improving the inhibitor.Semantic proximity Read ↗

Expression and purification of recombinant human alpha1-proteinase inhibitor and its single amino acid substituted variants in Escherichia coli for enhanced stability and biological activity.Semantic proximity Read ↗

Oxidation resistant muteins of antileukoproteinase as potential therapeutic agents.Semantic proximity Read ↗

Characterization of human pre-elafin mutants: full antipeptidase activity is essential to preserve lung tissue integrity in experimental emphysema.Semantic proximity Read ↗

Inhibitors of proprotein convertasesSemantic proximity Read ↗

Comparison of the properties of rare variants of alpha1-proteinase inhibitor expressed in COS-1 cells and assessment of their potential as risk factors in human disease.Semantic proximity Read ↗

Alpha 1-antitrypsin variants produced by recombinant DNA: differences in elastase inhibitory activity and resistance to oxidant agents.Semantic proximity Read ↗

Mutations on the hinge region of leukocyte elastase inhibitor determine the loss of inhibitory function.Semantic proximity Read ↗

SLPI and elafin: multifunctional antiproteases of the WFDC familySemantic proximity Read ↗

Single amino acid substitutions in recombinant plant-derived human α1-proteinase inhibitor confer enhanced stability and functional efficacy.Semantic proximity Read ↗

Application of directed evolution and back-to-consensus algorithms to human alpha1-antitrypsin leads to diminished anti-protease activity and augmented anti-inflammatory activities.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.